Reworking of the genetic code enabled biological methane and carbon dioxide formation from methylamines

FUEL 182

Joseph A. Krzycki, krzycki.1@osu.edu, The Department of Microbiology, The Ohio State University, 484 West 12th Ave, Columbus, OH 43210
Biological methanogenesis from monomethylamine, dimethylamine, or trimethylamine is initiated by one of three methyltransferases that methylate a cognate corrinoid protein with a specific methylamine. Each methylamine methyltransferase contains an unusual electrophilic residue, pyrrolysine. Pyrrolysine is inserted during translation under the direction of an amber (TAG=UAG) codon found in each methyltransferase gene. UAG translation as pyrrolysine requires a pyrrolysine-specific tRNA and pyrrolysyl-tRNA synthetase. Pyrrolysine biosynthesis and the genetic encoding of pyrrolysine in total requires only five gene products, and these are readily transmissible to a naïve organism. Methylamine methyltransferase lacking pyrrolysine, due to either site-directed mutagenesis, or pyrrolysine modification, have greatly diminished activity in methylating corrinoid cofactors. These results suggest that methane formation from methylamines requires pyrrolysine as an essential catalytic residue; a result that is consistent with proposed models of pyrrolysine-containing methyltransferase catalysis during Co(I)corrinoid methylation with methylamines.